SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P81065

- GST_OCHAN

UniProt

P81065 - GST_OCHAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutathione S-transferase

Gene
gst
Organism
Ochrobactrum anthropi
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication

Kineticsi

  1. KM=0.132 mM for glutathione1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101Glutathione
Binding sitei35 – 351Glutathione
Binding sitei52 – 521Glutathione; via amide nitrogen and carbonyl oxygen
Binding sitei105 – 1051Glutathione

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase (EC:2.5.1.18)
Gene namesi
Name:gst
OrganismiOchrobactrum anthropi
Taxonomic identifieri529 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101C → A: Strongly reduced affinity for glutathione. Reduces enzyme activity by about 50%. 1 Publication
Mutagenesisi11 – 111S → A: Reduced activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201Glutathione S-transferasePRO_0000185973Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54
Helixi12 – 2110
Beta strandi26 – 294
Turni32 – 354
Helixi43 – 453
Beta strandi54 – 585
Beta strandi61 – 655
Helixi66 – 7510
Helixi80 – 823
Helixi89 – 10921
Helixi110 – 1123
Helixi118 – 13821
Beta strandi148 – 1503
Helixi153 – 16715
Helixi176 – 18611
Helixi189 – 1979

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NTOX-ray2.10A1-201[»]
2PVQX-ray1.80A1-201[»]
ProteinModelPortaliP81065.
SMRiP81065. Positions 1-201.

Miscellaneous databases

EvolutionaryTraceiP81065.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8181GST N-terminalAdd
BLAST
Domaini87 – 201115GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni65 – 662Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Beta family.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF13409. GST_N_2. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P81065-1 [UniParc]FASTAAdd to Basket

« Hide

MKLYYKVGAC SLAPHIILSE AGLPYELEAV DLKAKKTADG GDYFAVNPRG    50
AVPALEVKPG TVITQNAAIL QYIGDHSDVA AFKPAYGSIE RARLQEALGF 100
CSDLHAAFSG LFAPNLSEEA RAGVIANINR RLGQLEAMLS DKNAYWLGDD 150
FTQPDAYASV IIGWGVGQKL DLSAYPKALK LRERVLARPN VQKAFKEEGL 200
N 201
Length:201
Mass (Da):21,739
Last modified:May 30, 2000 - v2
Checksum:i763B2D3DECA21F2D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y17279 Genomic DNA. Translation: CAA76728.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y17279 Genomic DNA. Translation: CAA76728.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2NTO X-ray 2.10 A 1-201 [» ]
2PVQ X-ray 1.80 A 1-201 [» ]
ProteinModelPortali P81065.
SMRi P81065. Positions 1-201.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P81065.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF13409. GST_N_2. 1 hit.
[Graphical view ]
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning, expression and site-directed mutagenesis of glutathione S-transferase from Ochrobactrum anthropi."
    Favaloro B., Tamburro A., Angelucci S., de Luca A., di Ilio C., Rotilio D.
    Biochem. J. 335:573-579(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25 AND 50-74, MUTAGENESIS.
  2. "Purification and characterization of a novel glutathione transferase from Ochrobactrum anthropi."
    Favaloro B., Melino S., Petruzzelli R., di Ilio C., Rotilio D.
    FEMS Microbiol. Lett. 160:81-86(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-25.
  3. "Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site."
    Allocati N., Federici L., Masulli M., Favaloro B., Di Ilio C.
    Proteins 71:16-23(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-10, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiGST_OCHAN
AccessioniPrimary (citable) accession number: P81065
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 30, 2000
Last modified: June 11, 2014
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi